Inhibition by vesicular stomatitis virus of herpes simplex virus-directed protein synthesis

Abstract

Infection of mammalian cells with either herpes simplex virus (HSV) or vesicular stomatitis virus (VSV) results in a marked inhibition of host protein synthesis. These viruses employ different mechanisms to turn off the host. In previous studies we showed that following infection with HSV, cellular mRNA was degraded and host polyribosomes were dissociated (Nishioka and Silverstein, Proc. Nat. Acad. Sci. USA 74, 2370-2374, 1977; Nishioka and Silverstein, J. Virol. 25, 422-426, 1978a). Degradation required synthesis of an HSV-specified polypeptide whereas dissociation appeared to be mediated by a heat-labile virion associated function (Nishioka and Silverstein, J. Virol. 27, 619-627, 1978b). In contrast, when cells are infected with VSV, host mRNAs are not degraded and polyribosome profiles are not drastically altered (Nishioka and Silverstein, 1978a). We have exploited the properties of these two viruses by infecting cells either simultaneously or sequentially in an effort to test our previous hypotheses. Analyses of the distribution of polyribosomes, stability of mRNA, synthesis of mRNA, and patterns of protein synthesis in coinfected cells permit us to conclude that dissociation of polyribosomes in cells infected with HSV results from expression of a virion associated function, degradation of cellular mRNA requires expression of the HSV genome, and VSV is dominant in doubly infected cells because it inhibits de novo transcription of the HSV genome.